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Database: UniProt
Entry: H1VV68_COLHI
LinkDB: H1VV68_COLHI
Original site: H1VV68_COLHI 
ID   H1VV68_COLHI            Unreviewed;       787 AA.
AC   H1VV68;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=CH063_13627 {ECO:0000313|EMBL:CCF44127.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF44127.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC       ECO:0000256|RuleBase:RU000394}.
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DR   EMBL; CACQ02006644; CCF44127.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1VV68; -.
DR   STRING; 759273.H1VV68; -.
DR   EnsemblFungi; CCF44127; CCF44127; CH063_13627.
DR   VEuPathDB; FungiDB:CH63R_08938; -.
DR   eggNOG; KOG0245; Eukaryota.
DR   HOGENOM; CLU_001485_2_3_1; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd22705; FHA_KIF1; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   PANTHER; PTHR47117:SF1; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}.
FT   DOMAIN          1..326
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          588..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          728..778
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         73..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   787 AA;  86787 MW;  1DDDAB4D71A0C3E1 CRC64;
     MKDNQTILAT PPDAHTKNAK DAGQKVFAFD RSYWSFDRKD SHYAGQDNLF DDLGQPLLDN
     AFGGYNNCIF AYGQTGSGKS YSMMGYGKEV GIIPNICQDM FKRITALQED KNLRCTVEVS
     YLEIYNERVR DLLNPSTKGN LKVREHPSTG PYVEDLAKLV VGSFQEIEHL MDEGNKARTV
     AATNMNETSS RSHAVFTLML TQKKFDPETK MEMEKVAKIS LVDLAGSERA TSTGATGARL
     KEGAEINRSL SSLGRVISAL ADISTGKKKK GPGGQVPYRD SVLTWLLKDS LGGNSMTAMI
     AAISPADINY DETLSTLRYA DSAKRIKNHA VVNEDANARM IRELKEELAL LRNQLGGGGG
     GGTAGATGGA AGGVVTSEEV YPEGTPLEKQ FVSITSSDGA VKKVSKAEIA EQLNQSEKLL
     TDLNQTWEQK LAKTEEIHKE REAALEELGI SIEKGFIGLS TPKKMPHLVN LSDDPLLAEC
     LVYNLKPGLT TVGNMDTNAD NQANIRLNGT RILHDHCAFE NGPDGTVMVI PSEGASVMVN
     GKRIEEPKQL HSGYRVILGD FHIFRFNHPM EAQKERADKS LLRQSVTASQ LQSLEKSIPT
     PAVSPRPGHE RNWSKTGSDI GDSRPDSPIP FRTGRDNDWS FARREAAEAI LGTNQNLASL
     TDEELNALFE GIQRARAERV NGREGDDDAE SVTSYPIREK YMSTGTLDNF SLDTALTMPS
     TPKQGEVDDK LREVREEMQS QLDRQKEEYQ DQLKTAEAAN VEQQLEVQRR QFEEKLEKMD
     PLKRTKG
//
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